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• W2110564533 endingPage "945" @default.
• W2110564533 startingPage "933" @default.
• W2110564533 abstract "ABSTRACT The MMPs constitute a family of endopeptidases that can cleavage extracellular proteins. They are involved in a number of events; some of these include inflammatory processes. One of its targets is the TREM-1, which has emerged as an important modulator of innate immune responses in mammals. This transmembrane glycoprotein possesses an Ig-like ectodomain readily shed by MMPs to generate sTREM-1. Whereas membrane-anchored TREM-1 amplifies inflammatory responses, sTREM-1 exhibits anti-inflammatory properties. Here we show that sustained cell surface expression of TREM-1 in human monocytes, through metalloproteinase inhibition, counteracts the well-characterized down-regulation of several proinflammatory cytokines during the ET time-frame, also known as M2 or alternative activation. In addition to the cytokines profile, other features of the ET phenotype were underdeveloped when TREM-1 was stabilized at the cell surface. These events were mediated by the signal transducers PI3Ks and Syk. We also show that sTREM-1 counteracts the proinflammatory response obtained by membrane TREM-1 stabilization but failed to induce ET on naïve human monocytes. As the sustained TREM-1 expression at the cell surface suffices to block the progress of a refractory state in human monocytes, our data indicate that TREM-1 and MMPs orchestrate an “adaptive” form of innate immunity by modulating the human monocytes response to endotoxin." @default.
• W2110564533 created "2016-06-24" @default.
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• W2110564533 date "2012-06-01" @default.
• W2110564533 modified "2023-10-18" @default.
• W2110564533 title "Role of MMPs in orchestrating inflammatory response in human monocytes via a TREM-1-PI3K-NF-κB pathway" @default.
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• W2110564533 doi "https://doi.org/10.1189/jlb.0711340" @default.
• W2110564533 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22459945" @default.
• W2110564533 hasPublicationYear "2012" @default.
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